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<StructureSection load='1psa' size='340' side='right'caption='[[1psa]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='1psa' size='340' side='right'caption='[[1psa]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1psa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PSA FirstGlance]. <br>
<table><tr><td colspan='2'>[[1psa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PSA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0ZL:N-(ETHOXYCARBONYL)-L-LEUCYL-N-[(1R,2S,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]-L-LEUCINAMIDE'>0ZL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pepsin_A Pepsin A], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.1 3.4.23.1] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0ZL:N-(ETHOXYCARBONYL)-L-LEUCYL-N-[(1R,2S,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]-L-LEUCINAMIDE'>0ZL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1psa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1psa OCA], [https://pdbe.org/1psa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1psa RCSB], [https://www.ebi.ac.uk/pdbsum/1psa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1psa ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1psa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1psa OCA], [https://pdbe.org/1psa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1psa RCSB], [https://www.ebi.ac.uk/pdbsum/1psa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1psa ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PEPA_PIG PEPA_PIG]] Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.  
[https://www.uniprot.org/uniprot/PEPA_PIG PEPA_PIG] Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1psa ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1psa ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure determination by molecular replacement methods of a monoclinic pepsin/renin inhibitor complex crystal, with two molecules in the asymmetric unit, is presented. The atomic model, consisting of two liganded pepsin molecules and 110 water molecules, has been refined to a final crystallographic R value of 0.139 for data between 8 and 2.9 A resolution. The structure reveals a previously undescribed pepsin dimer formed predominantly by polar interactions. Inhibitor binding induces global structural changes in the native enzyme similar, but not identical, to the ones observed in other chemically similar pepsin/renin inhibitor complexes crystallized in an orthorhombic form. A region of the polypeptide chain (residues 292-297) which was not visible in the orthorhombic crystal is well ordered in the presently described structure; possibly induced by crystal contacts. The crystal packing of native pepsin is compared with the two different crystal forms of the inhibited enzyme.
Structure of a pepsin/renin inhibitor complex reveals a novel crystal packing induced by minor chemical alterations in the inhibitor.,Chen L, Erickson JW, Rydel TJ, Park CH, Neidhart D, Luly J, Abad-Zapatero C Acta Crystallogr B. 1992 Aug 1;48 ( Pt 4):476-88. PMID:1418819<ref>PMID:1418819</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1psa" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Pepsin|Pepsin]]
*[[Pepsin|Pepsin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pepsin A]]
[[Category: Sus scrofa]]
[[Category: Pig]]
[[Category: Abad-Zapatero C]]
[[Category: Abad-Zapatero, C]]
[[Category: Chen L]]
[[Category: Chen, L]]
[[Category: Acid proteinase]]
[[Category: Hydrolase-hydrolase inhibitor complex]]

Revision as of 05:58, 17 April 2024

STRUCTURE OF A PEPSIN(SLASH)RENIN INHIBITOR COMPLEX REVEALS A NOVEL CRYSTAL PACKING INDUCED BY MINOR CHEMICAL ALTERATIONS IN THE INHIBITOR

1psa, resolution 2.90Å

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